According to SDAP (structural database of allergenic proteins, http://fermi.utmb.edu/), storage 11S and 7S globulins from seeds of peanut, soybean and some other plants are allergens. A -barrel conjoined with a group of -helices represents the structural basis of domains of the two-domain 11S and 7S seed storage globulins. During evolution, extended disordered inserts of enhanced susceptibility to proteolytic attack appeared in the amino acid sequences of storage globulins outside the -barrel--helix structural module. Regularities of storage globulin limited proteolysis during seed germination and in vitro are determined by these inserts. In this review, available information on successive reactions of limited proteolysis specific to 11S and 7S globulins from peanut, soybean and some other plants is collected. It was demonstrated that limited proteolysis of 11S globulin from peanut (A. Cherdivară et al., 2017) calls forth destruction of a C-terminal region of - chains, including the region forming the group of -helices. Three of the four antigen determinants (IgE epitopes) identified in the peanut subunit Ara h3 (P. Rabjohn et al., 1999) belong to this region. Thus, the limited proteolysis leads to a significant decrease in the allergenicity level of the subunit Ara h3. The presence of IgE epitopes in homologous regions of conserved sequences of -helices from most other subunits of the peanut 11S globulin, non-identical to Ara h3, is very probable. Thus, the limited proteolysis of not only the Ara h3 subunit, but also the whole hetero-hexamer molecule of peanut 11S globulin can be accompanied by a significant decrease in the level of its allergenicity. Prospects for reducing allergenicity of soybean 11S globulin by limited proteolysis are not so unambiguous. On the one hand, the limited proteolysis of the subunit Gly m G1 leads to the destruction of the C-terminal region of the -chains (A. Shutov et al., 2012), where both identified IgE epitopes are present (T.A. Beardslee et al., 2000). On the other hand, only one of the IgE epitopes identified in the Gly m G2 subunit (R.M. Helm et al., 2000) can be removed using limited proteolysis of this protein (A. Shutov et al., 1993). The detachment of the -chain -helices during limited proteolysis of several other 11S globulins was observed as well. A high degree of conservation of this region in the primary structures of 11S globulins allows suggesting the presence of IgE epitopes, similar to those identified in peanut and soybean 11S globulins, in many other storage proteins of the 11S globulin family. Prospects for the reduction of allergenicity of seed 7S globulins by limited proteolysis are advantageous as well. Limited proteolysis of peanut 7S globulin Ara h1 starts with complete destruction of a disordered N-terminal extension (A. Cherdivară et al., 2016), which contains one third of IgE epitopes identified in the amino acid sequence of this protein (D.S. Shin et al., 1998). Further limited proteolysis calls fourth destruction of another disordered region inside the N-terminal domain that contains an additional IgE epitope identified in the Ara h1 sequence. Summary information considered in the review on the structure of seed storage globulins, as well as on the IgE epitopes identified in their amino acid sequences, evidences the availability of limited proteolysis as a means of considerable reduction of the level of allergenicity, not only of peanut and soybean 11S and 7S globulins, but also of those from other plants whose seeds are used as food either directly or as additives to various food products.